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J. Biol. Chem., Vol. 277, Issue 41, 38121-38126, October 11, 2002
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From the Department of Pharmacology, University of North Carolina
School of Medicine, Chapel Hill, North Carolina 27599-7365
Members of the vasodilator-stimulated
phosphoprotein (VASP) family are important regulators of actin
cytoskeletal dynamics whose functions and protein-protein interactions
are regulated by phosphorylation by the cAMP-dependent
protein kinase (PKA). Herein, we show that phosphorylation of VASP is
dynamically regulated by cellular adhesion to extracellular matrix.
Detachment of cells stimulated PKA activity and induced
PKA-dependent phosphorylation of VASP and the related
murine-Enabled (Mena) protein. VASP and Mena were rapidly
dephosphorylated immediately following reattachment but showed an
intermediate level of phosphorylation during active cell spreading.
This pattern correlated closely with adhesion-dependent changes in PKA activity. The in vivo interaction of VASP
with the Abl tyrosine kinase, shown here for the first time, was
readily apparent in adherent cells, lost following cellular detachment, and induced upon reattachment to matrix. Importantly, inhibition of PKA
activity prevented phosphorylation of VASP and dissociation of VASP-Abl
complexes after cellular detachment, whereas activation of PKA
completely eliminated the co-immunoprecipitation of Abl activity with
VASP. These data establish a new biochemical link between cell adhesion
and regulation of VASP proteins and provide the first demonstration of
a regulated interaction between VASP and Abl in mammalian cells.
Regulation of Vasodilator-stimulated Phosphoprotein
Phosphorylation and Interaction with Abl by Protein Kinase A and
Cell Adhesion*
,
*
This work was supported by NCI National Institutes of Health
Grant CA92237 (to A. K. H.) and National Institutes of Health Grants
HL45100 and GM26165 (to R. L. J.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pharmacology,
Campus Box 7365, University of North Carolina School of Medicine,
Chapel Hill, North Carolina 27599-7365. Tel.: 919-968-8791; Fax:
919-966-5640; E-mail: Alan_Howe@med.unc.edu.
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